Membrane system within the cytoplasm of a eukaryotic cell (see eukaryote), important in the synthesis of proteins and lipids. The ER usually makes up more than half the membrane of the cell and is continuous with the outer membrane of the nuclear envelope (see nucleus). There are two distinct regions of ER: the rough ER, or RER (so called because of the protein-synthesizing ribosomes attached to it), and the smooth ER (SER), which is not associated with ribosomes and is involved in the synthesis of lipids and the detoxification of some toxic chemicals.
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These structures are responsible for several specialized functions: protein translation, folding and transport of proteins to be used in the cell membrane (e.g. transmembrane receptors and other integral membrane proteins), or to be secreted (exocytosed) from the cell (e.g. digestive enzymes); sequestration of calcium; and production and storage of glycogen, steroids, and other macromolecules. The endoplasmic reticulum is part of the endomembrane system. The basic structure and composition of the ER membrane is similar to the plasma membrane.
The general structure of the endoplasmic reticulum is an extensive membrane network of cisternae (sac-like structures) held together by the cytoskeleton. The phospholipid membrane encloses a space, the cisternal space (or lumen), from the cytosol. The functions of the endoplasmic reticulum vary greatly depending on the exact type of endoplasmic reticulum and the type of cell in which it resides. The three varieties are called rough endoplasmic reticulum, smooth endoplasmic reticulum, and sarcoplasmic reticulum.
The quantity of RER and SER in a cell can quickly interchange from one type to the other, depending on changing metabolic needs: one type will undergo numerous changes including new proteins embedded in the membranes in order to transform. Also, massive changes in the protein content can occur without any noticeable structural changes, depending on the enzymatic needs of the cell (as per the functions listed below).
The membrane of the rough endoplasmic reticulum is continuous with the outer layer of the nuclear envelope. Although there is no continuous membrane between the rough ER and the Golgi apparatus, membrane bound vesicles shuttle proteins between these two compartments. COP II brings vesicles to the golgi and COP I brings the membrane back. The rough endoplasmic reticulum works in concert with the Golgi complex to target new proteins to their proper destinations.
The RER is key in producing
Correct folding of newly-made proteins is made possible by several endoplasmic reticulum chaperone proteins, including protein disulfide isomerase (PDI), ERp29, the Hsp70 family member Grp78, calnexin, calreticulin, and the peptidylpropyl isomerase family. Only properly-folded proteins are transported from the rough ER to the Golgi complex.
The endoplasmic reticulum is also part of a protein sorting pathway. It is, in essence, the transportation system of the eukaryotic cell. The majority of endoplasmic reticulum resident proteins are retained in the endoplasmic reticulum through a retention motif. This motif is composed of four amino acids at the end of the protein sequence. The most common retention sequence is KDEL (lys-asp-glu-leu). However, variation on KDEL does occur and other sequences can also give rise to endoplasmic reticulum retention. It is not known if such variation can lead to sub-endoplasmic reticulum localizations. There are three KDEL receptors in mammalian cells, and they have a very high degree of sequence identity. The functional differences between these receptors remain to be established.
Dietary energy tissue-specifically regulates endoplasmic reticulum chaperone gene expression in the liver of mice
Sep 01, 1997; Dietary Energy Tissue-Specifically Regulates Endoplasmic Reticulum Chaperone Gene Expression in the Liver of Mice"2 Joseph M....
PI3K/Akt Promotes GRP78 Accumulation and Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis in HEK293 Cells
Mar 01, 2010; Abstract. The potential pro-survival role of phosphatidylinositol 3-kinase (PI3K)/Akt during endoplasmic reticulum stress has...